ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    ISSN: 1432-0827
    Keywords: calmodulin ; calcium ; mineralisation ; tooth germ
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Calmodulin, a calcium binding protein, has been implicated in the regulation of many calcium-dependent biological processes. Since calcium has an important role in hard tissue genesis, both at intra- and extracellular levels, we anticipate that calcium binding proteins may modulate this process. The present study investigated a mineralising tissue, the rat molar tooth germ, to determine the presence of calmodulin-like activity. A heat-treated cell-free extract of tooth germs provided enhancement of Ca2+-dependent Mg2+-ATPase and 3′:5′-nucleotide phosphodiesterase activity. No enhancement occurred in the absence of calcium or in the presence of trifluoperazine. SDS-polyacrylamide gel electrophoresis of this extract revealed a protein band of approximately 18,000 mol. wt. These findings indicate the presence of calmodulin-like activity in rat molar tooth germs and support the proposal that calcium and calcium binding proteins, in particular calmodulin, have a major regulatory role in the biology of mineralising tissues.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 1868-1874 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1432-0878
    Keywords: Calbindin Calcium-binding protein Calcium signalling Nuclear-cytoplasmic partitioning Rat (Sprague Dawley; Wistar) Mouse (CB28-nullmutant; C57BL6)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Recent attempts to understand the function of calbindin28kDa, a widely expressed calcium-binding protein, are confounded by uncertainties over its subcellular location. Using immunoblot analysis of rat brain subregions, we found that the proportion of particulate calbindin28kDa (24–43% of total) was independent of expression level and location. The association of calbindin28kDa with particulate structures appeared to be specific, since it persisted when soluble calbindin28kDa was sequestered by antibodies added before tissue disruption. Moreover, when exogenous calbindin28kDa was added during homogenisation of brain from calbindin28kDa-nullmutant mice, only 10% partitioned to the particulate fraction compared with 33% of endogenous calbindin28kDa in wild-type controls. Confocal microscopy showed that calbindin28kDa was predominantly extranuclear in all tissues analysed (i.e. various brain regions, isolated neurons, and dental enamel epithelium). Dual-label microscopy of neural dense particulate fractions confirmed the extranuclear location of calbindin28kDa and also showed that it partly colocalised with synaptosome and microtubule markers. Using sucrose step gradients, calbindin28kDa was separated from nuclei in parallel with synaptosome and endoplasmic reticulum markers. However, no association with the marker proteins (synaptophysin, ERp29, α/β-tubulin) was detected by calbindin28kDa-immunoprecipitation analysis. Together these findings provide the first consistent picture that calbindin28kDa is located predominantly outside of the nucleus, irrespective of tissue type (neuronal vs non-neuronal) and experimental approach (biochemical vs morphological). The evidence of a substantial, strong and specific association with insoluble cellular structures challenges the widely held view of calbindin28kDa as a mobile calcium buffer, and supports the existence of important alternative roles that involve target proteins.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1891-1900 
    ISSN: 0173-0835
    Keywords: Calcium ; Dental enamel ; Microscale ; Ligand overlays ; Two-dimensional polyacrylamide gel electrophoresis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Poor understanding of the molecular links between disturbed calcium regulation in cells and disease remains a problem of considerable biomedical importance. Dental enamel cells might provide useful insights to this problem since they handle calcium in bulk without suffering its cytotoxic effects. Two practical challenges hindered investigation of calcium handling mechanisms in enamel cells - paucity of molecular information and limited availability of sample from developing rat teeth, the experimental system of choice. This paper outlines the microscale proteomic approaches we applied to overcome these difficulties and reviews several major findings that ensued from initial characterization of the enamel cell proteome. Enamel cells are now established as a powerful model for fundamental calcium research and have provided outcomes of broad biological relevance, including the discovery of a new endoplasmic reticulum protein. Future proteomic approaches that might benefit understanding of function are discussed.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 5
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...